1RQ1
Structure of Ero1p, Source of Disulfide Bonds for Oxidative Protein Folding in the Cell
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE |
| Collection date | 2003-02-15 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 62 |
| Unit cell lengths | 106.200, 106.200, 124.300 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 50.000 - 2.800 |
| Rwork | 0.206 |
| R-free | 0.23800 |
| Structure solution method | MIR |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.752 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHARP |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 2.800 |
| Number of reflections | 19520 |
| <I/σ(I)> | 19.2 |
| Completeness [%] | 99.4 |
| Redundancy | 7.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.8 | 293 | cacodylate, cadmium chloride, sodium acetate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
